VRP1/YLR337C Literature Guide Help

Other names published for VRP1: END5, MDP2, YLR337W, verprolin, YLR337C

VRP1 - Non-Fungal Related Genes/Proteins (12)

ReferenceOther Genes Addressed
Meng L, et al.  (2007) Actin binding and proline rich motifs of CR16 play redundant role in growth of vrp1Delta cells. Biochem Biophys Res Commun 357(1):289-94
Thanabalu T, et al.  (2007) Verprolin function in endocytosis and actin organization. Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain. FEBS J 274(16):4103-25
Rajmohan R, et al.  (2006) WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain in the presence of WIP. Biochem Biophys Res Commun 342(2):529-36
Paunola E, et al.  (2002) WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett 513(1):92-7
Zettl M and Way M  (2002) The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs. Curr Biol 12(18):1617-22
Naqvi SN, et al.  (2001) Vrp1p functions in both actomyosin ring-dependent and Hof1p-dependent pathways of cytokinesis. Traffic 2(3):189-201
Evangelista M, et al.  (2000) A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J Cell Biol 148(2):353-62
Geli MI, et al.  (2000) An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J 19(16):4281-91
Vaduva G, et al.  (1999) The human WASP-interacting protein, WIP, activates the cell polarity pathway in yeast. J Biol Chem 274(24):17103-8
Miki H and Takenawa T  (1998) Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization. Biochem Biophys Res Commun 243(1):73-8
Naqvi SN, et al.  (1998) The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast. Curr Biol 8(17):959-62
Donnelly SF, et al.  (1993) A proline-rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae. Mol Microbiol 10(3):585-96